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Differential binding of tetrodotoxin and its derivatives to voltage-sensitive sodium channel subtypes (Nav 1.1 to Nav 1.7).

Tadaaki TsukamotoYukie ChibaMinoru WakamoriTomoshi YamadaShunsuke TsunogaeYuko ChoRyo SakakibaraTakuya ImazuShouta TokoroYoshiki SatakeMasaatsu AdachiToshio NishikawaMari Yotsu-YamashitaKeiichi Konoki
Published in: British journal of pharmacology (2017)
The reduced binding of chiriquitoxin to Nav 1.7 was attributed to its C11-OH and/or C12-NH2 , based on reported models for the TTX-VSSC complex. Chiriquitoxin is a useful tool for probing the configuration of the TTX binding site until a crystal structure for the mammalian VSSC is solved.
Keyphrases
  • crystal structure
  • dna binding
  • binding protein
  • single molecule
  • molecular dynamics simulations
  • transcription factor
  • perovskite solar cells